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DOI	10.1073/pnas.2109241118
	Partial synthetic models of FeMoco with sulfide and carbyne ligands: Effect of interstitial atom in nitrogenase active site
	Le L.N.V.; Bailey G.A.; Scott A.G.; Agapie T.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:49
英文摘要	Nitrogen-fixing organisms perform dinitrogen reduction to ammonia at an Fe-M (M = Mo, Fe, or V) cofactor (FeMco) of nitrogenase. FeMco displays eight metal centers bridged by sulfides and a carbide having the MFe7S8C cluster composition. The role of the carbide ligand, a unique motif in protein active sites, remains poorly understood. Toward addressing how the carbon bridge affects the physical and chemical properties of the cluster, we isolated synthetic models of subsite MFe3S3C displaying sulfides and a chelating carbyne ligand. We developed synthetic protocols for structurally related clusters, [TpM’Fe3S3X]n2, where M’ = Mo or W, the bridging ligand X = CR, N, NR, S, and Tp = Tris(3,5-dimethyl-1-pyrazolyl)hydroborate, to study the effects of the identity of the heterometal and the bridging X group on structure and electrochemistry. While the nature of M’ results in minor changes, the chelating, μ3-bridging carbyne has a large impact on reduction potentials, being up to 1 V more reducing compared to nonchelating N and S analogs. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Carbide clusters; FeMoco model; Iron-sulfur clusters; Nitrogenase; Reduction potential
语种	英语
scopus关键词	barban; carbon; iron; iron molybdenum cofactor; molybdenum; nitrogen; nitrogenase; sulfide; sulfur; tetrahydrofuran; unclassified drug; barban; carbamic acid derivative; iron; ligand; molybdenum; molybdenum iron protein; nitrogenase; sulfide; Article; atom; chelation; chemical structure; controlled study; cyclic voltammetry; diffusion; electrochemistry; filtration; model; oxidation reduction potential; oxidation reduction state; precipitation; synthesis; X ray diffraction; chemistry; enzyme active site; metabolism; molecular model; nitrogen fixation; oxidation reduction reaction; physiology; X ray crystallography; Carbamates; Carbon; Catalytic Domain; Crystallography, X-Ray; Iron; Ligands; Models, Molecular; Molecular Structure; Molybdenum; Molybdoferredoxin; Nitrogen; Nitrogen Fixation; Nitrogenase; Oxidation-Reduction; Sulfides; Sulfur
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/250951
作者单位	Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, United States
推荐引用方式 GB/T 7714	Le L.N.V.,Bailey G.A.,Scott A.G.,et al. Partial synthetic models of FeMoco with sulfide and carbyne ligands: Effect of interstitial atom in nitrogenase active site[J],2021,118(49).
APA	Le L.N.V.,Bailey G.A.,Scott A.G.,&Agapie T..(2021).Partial synthetic models of FeMoco with sulfide and carbyne ligands: Effect of interstitial atom in nitrogenase active site.Proceedings of the National Academy of Sciences of the United States of America,118(49).
MLA	Le L.N.V.,et al."Partial synthetic models of FeMoco with sulfide and carbyne ligands: Effect of interstitial atom in nitrogenase active site".Proceedings of the National Academy of Sciences of the United States of America 118.49(2021).